肺泡界面活性劑中的主成分dipalmitoyl phosphatidylcholine （DPPC）被認為是降低肺泡內襯液層表面張力的主要成分，但DPPC價格昂貴。利用擁有兩條雙十六碳鏈，結構與DPPC相似的hexadecyltrimethylammonium-hexadecylsulfate （HTMA-HS）進行單分子層實驗。結果顯示崩潰表面壓能達到72.0 mN/m，表示此時界面上的表面張力接近零。由上述結果發現HTMA-HS有取代DPPC做為肺泡界面活性劑之主要物質並用於治療呼吸窘迫症的潛力，但HTMA-HS容易隨albumin離開界面，導致界面上自由HTMA-HS分子的損失，使HTMA-HS的動態界面活性受到抑制。本研究分別以1,2-二棕櫚醯基-sn-甘油-3-磷酸乙醇胺-N-[（甲氧基）聚乙烯醇-1000]（DPPE-PEG1000）、L-A-磷酸鹽（DPPE）及聚乙烯吡咯烷酮（polyvinylpyrrolidone, PVP）為添加劑，來改善HTMA-HS易與albumin作用而從氣液界面上損失的情形。利用表面壓-面積等溫線的量測，配合螢光顯微鏡法（fluorescence microscopy, FM）探討於連續來回壓縮-擴張界面的條件下，液相中牛血清白蛋白（bovine serum albumin, BSA）對不同混合分子層動態界面活性的影響，並探討聚乙二醇（PEG）及其長度對於避免蛋白質再吸附的效果。結果顯示添加1 mol%、3 mol%及10 mol%的DPPE或DPPE-PEG1000，都無法有效減少HTMA-HS單分子層的損失率。比較HTMA-HS/DPPE/albumin、HTMA-HS/DPPE-PEG1000/albumin及文獻中HTMA-HS/DPPE-PEG2000/albumin混合系統的結果，結果顯示PEG鏈確實可以避免albumin在擴張過程的再吸附。比較DPPE-PEG1000/albumin與文獻中DPPE-PEG2000/albumin的結果，顯示當PEG鏈愈長時，albumin在擴張過程中愈不易再吸附到界面上，對albumin有愈大的排斥效應或產生愈顯著的立體障礙。由上述的結果可以歸納出PEG對分子損失的影響因素有溶解度、對混合單分子層排列的影響，以及對蛋白質的排斥效應或產生的立體障礙。較長的PEG鏈，溶解度較大，對混合單分子層的排列影響較大，使混合單分子層在壓縮過程中容易脫附，但較不平坦的表面會使albumin不易再吸附到界面上，且當albumin靠近時，對其產生的排斥行為也愈顯著。在HTMA-HS/PVP/albumin混合系統中，所添加的PVP會對albumin產生排斥效應，可以避免albumin於擴張過程中的再吸附行為，減少分子損失。但由於PVP是屬於水溶性的物質，在壓縮過程中會從界面上脫附。因此添加過多的PVP，會使在壓縮過程中，吸附在界面上的分子數減少，所以無法到達較高的表面壓，而無法減少分子損失的情形。

In this study, the effects of bovine serum albumin (BSA) on the mixed Langmuir monolayer behavior of hexadecyltrimethylammonium-hexadecylsulfate (HTMA-HS), with dipalmitoyl phosphatidylethanolamine-polyethylene glycol 1000 (DPPE-PEG1000), 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine (DPPE), and polyvinylpyrrolidone (PVP), respectively, were investigated by the Langmuir trough approach. Cyclic compression-expansion isotherms of the monolayers were examined to elucidate the induced removal characteristic of the molecules at the air/liquid interface. For mixed monolayers of HTMA-HS with adsorbed BSA at the cyclic interface, HTMA-HS would leave the interface with BSA during the interface compression stage, causing the loss of HTMA-HS at the interface. Comparing the results of mixed HTMA-HS/DPPE-PEG1000/BSA and HTMA-HS/DPPE/BSA monolayers, it is inferred that PEG chains were helpful in preventing the readsorption of BSA during the interface expansion stage. This property can be attributed to its segmental flexibility and its polar but uncharged chemical composition. The segmental flexibility results in high degree of steric exclusion at PEG-water interfaces, which in turn leads to protein resistance. The addition of hydrophilic polymer, PVP, could reduce the inhibition effect of BSA. This is because PVP could exert repulsive force on BSA when BSA approached the interface during the interface expansion stage.

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